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Entry version 183 (31 Jul 2019)
Sequence version 1 (01 Aug 1991)
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Protein

DNA-directed RNA polymerase I subunit RPA135

Gene

RPA135

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. RPA190 and RPA135 both contribute to the polymerase catalytic activity and together form the Pol I active center. In addition, subunit RPA12 contributes a catalytic zinc ribbon that is required for RNA cleavage by Pol I. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA190 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition.3 Publications

Miscellaneous

Three distinct zinc-containing RNA polymerases are found in eukaryotic nuclei: polymerase I for the ribosomal RNA precursor, polymerase II for the mRNA precursor, and polymerase III for 5S and tRNA genes.
Present with 14100 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri1104 – 1131C4-typeAdd BLAST28

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionNucleotidyltransferase, Transferase
Biological processRibosome biogenesis, Transcription
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-34172-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-73762 RNA Polymerase I Transcription Initiation
R-SCE-73772 RNA Polymerase I Promoter Escape

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA-directed RNA polymerase I subunit RPA135 (EC:2.7.7.6)
Alternative name(s):
DNA-directed RNA polymerase I 135 kDa polypeptide
Short name:
A135
DNA-directed RNA polymerase I polypeptide 2
Short name:
RNA polymerase I subunit 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RPA135
Synonyms:RPA2, RRN2, SRP3
Ordered Locus Names:YPR010C
ORF Names:YP9531.03C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XVI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YPR010C

Saccharomyces Genome Database

More...
SGDi
S000006214 RPA135

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1104C → A: No effect; when associated with A-1107; A-1128 and A-1131. 1 Publication1
Mutagenesisi1107C → A: Lethal. Abolishes recruitment of RPA1 to Pol I. No effect; when associated with A-1104; A-1128 and A-1131. 1 Publication1
Mutagenesisi1127C → R: Responsible of suppression of RPA190-5 and RPA190-1 mutations. 1
Mutagenesisi1128C → A: No effect; when associated with A-1104; A-1107 and A-1131. 1 Publication1
Mutagenesisi1131C → A: No effect; when associated with A-1104; A-1107 and A-1128. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000480802 – 1203DNA-directed RNA polymerase I subunit RPA135Add BLAST1202

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1
Modified residuei81PhosphoserineCombined sources1
Modified residuei1156PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P22138

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P22138

PRoteomics IDEntifications database

More...
PRIDEi
P22138

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P22138

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA.

6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
RPA190P109644EBI-15736,EBI-15730

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
36188, 161 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1664 DNA-directed RNA Polymerase I complex

Database of interacting proteins

More...
DIPi
DIP-135N

Protein interaction database and analysis system

More...
IntActi
P22138, 60 interactors

Molecular INTeraction database

More...
MINTi
P22138

STRING: functional protein association networks

More...
STRINGi
4932.YPR010C

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11203
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P22138

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RNA polymerase beta chain family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1104 – 1131C4-typeAdd BLAST28

Keywords - Domaini

Zinc-finger

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000183132

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000222963

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P22138

KEGG Orthology (KO)

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KOi
K03002

Identification of Orthologs from Complete Genome Data

More...
OMAi
FFGVVHY

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00653 RNA_pol_B_RPB2, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.270.10, 1 hit
2.40.50.150, 1 hit
3.90.1110.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR015712 DNA-dir_RNA_pol_su2
IPR007120 DNA-dir_RNAP_su2_dom
IPR037033 DNA-dir_RNAP_su2_hyb_sf
IPR007121 RNA_pol_bsu_CS
IPR007644 RNA_pol_bsu_protrusion
IPR007642 RNA_pol_Rpb2_2
IPR037034 RNA_pol_Rpb2_2_sf
IPR007645 RNA_pol_Rpb2_3
IPR007641 RNA_pol_Rpb2_7
IPR014724 RNA_pol_RPB2_OB-fold
IPR009674 Rpa2_dom_4

The PANTHER Classification System

More...
PANTHERi
PTHR20856 PTHR20856, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06883 RNA_pol_Rpa2_4, 1 hit
PF04563 RNA_pol_Rpb2_1, 1 hit
PF04561 RNA_pol_Rpb2_2, 1 hit
PF04565 RNA_pol_Rpb2_3, 1 hit
PF00562 RNA_pol_Rpb2_6, 1 hit
PF04560 RNA_pol_Rpb2_7, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01166 RNA_POL_BETA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P22138-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKVIKPPGQ ARTADFRTLE RESRFINPPK DKSAFPLLQE AVQPHIGSFN
60 70 80 90 100
ALTEGPDGGL LNLGVKDIGE KVIFDGKPLN SEDEISNSGY LGNKLSVSVE
110 120 130 140 150
QVSIAKPMSN DGVSSAVERK VYPSESRQRL TSYRGKLLLK LKWSVNNGEE
160 170 180 190 200
NLFEVRDCGG LPVMLQSNRC HLNKMSPYEL VQHKEESDEI GGYFIVNGIE
210 220 230 240 250
KLIRMLIVQR RNHPMAIIRP SFANRGASYS HYGIQIRSVR PDQTSQTNVL
260 270 280 290 300
HYLNDGQVTF RFSWRKNEYL VPVVMILKAL CHTSDREIFD GIIGNDVKDS
310 320 330 340 350
FLTDRLELLL RGFKKRYPHL QNRTQVLQYL GDKFRVVFQA SPDQSDLEVG
360 370 380 390 400
QEVLDRIVLV HLGKDGSQDK FRMLLFMIRK LYSLVAGECS PDNPDATQHQ
410 420 430 440 450
EVLLGGFLYG MILKEKIDEY LQNIIAQVRM DINRGMAINF KDKRYMSRVL
460 470 480 490 500
MRVNENIGSK MQYFLSTGNL VSQSGLDLQQ VSGYTVVAEK INFYRFISHF
510 520 530 540 550
RMVHRGSFFA QLKTTTVRKL LPESWGFLCP VHTPDGSPCG LLNHFAHKCR
560 570 580 590 600
ISTQQSDVSR IPSILYSLGV APASHTFAAG PSLCCVQIDG KIIGWVSHEQ
610 620 630 640 650
GKIIADTLRY WKVEGKTPGL PIDLEIGYVP PSTRGQYPGL YLFGGHSRML
660 670 680 690 700
RPVRYLPLDK EDIVGPFEQV YMNIAVTPQE IQNNVHTHVE FTPTNILSIL
710 720 730 740 750
ANLTPFSDFN QSPRNMYQCQ MGKQTMGTPG VALCHRSDNK LYRLQTGQTP
760 770 780 790 800
IVKANLYDDY GMDNFPNGFN AVVAVISYTG YDMDDAMIIN KSADERGFGY
810 820 830 840 850
GTMYKTEKVD LALNRNRGDP ITQHFGFGND EWPKEWLEKL DEDGLPYIGT
860 870 880 890 900
YVEEGDPICA YFDDTLNKTK IKTYHSSEPA YIEEVNLIGD ESNKFQELQT
910 920 930 940 950
VSIKYRIRRT PQIGDKFSSR HGQKGVCSRK WPTIDMPFSE TGIQPDIIIN
960 970 980 990 1000
PHAFPSRMTI GMFVESLAGK AGALHGIAQD STPWIFNEDD TPADYFGEQL
1010 1020 1030 1040 1050
AKAGYNYHGN EPMYSGATGE ELRADIYVGV VYYQRLRHMV NDKFQVRSTG
1060 1070 1080 1090 1100
PVNSLTMQPV KGRKRHGGIR VGEMERDALI GHGTSFLLQD RLLNSSDYTQ
1110 1120 1130 1140 1150
ASVCRECGSI LTTQQSVPRI GSISTVCCRR CSMRFEDAKK LLTKSEDGEK
1160 1170 1180 1190 1200
IFIDDSQIWE DGQGNKFVGG NETTTVAIPF VLKYLDSELS AMGIRLRYNV

EPK
Length:1,203
Mass (Da):135,742
Last modified:August 1, 1991 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i72FA95B66F98C5F8
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U31900 Genomic DNA Translation: AAA97589.1
M62804 Genomic DNA Translation: AAA34993.1
Z49919 Genomic DNA Translation: CAA90154.1
Z71255 Genomic DNA Translation: CAA95050.1
BK006949 Genomic DNA Translation: DAA11437.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A39607

NCBI Reference Sequences

More...
RefSeqi
NP_015335.1, NM_001184107.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YPR010C_mRNA; YPR010C_mRNA; YPR010C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
856119

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YPR010C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31900 Genomic DNA Translation: AAA97589.1
M62804 Genomic DNA Translation: AAA34993.1
Z49919 Genomic DNA Translation: CAA90154.1
Z71255 Genomic DNA Translation: CAA95050.1
BK006949 Genomic DNA Translation: DAA11437.1
PIRiA39607
RefSeqiNP_015335.1, NM_001184107.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C2MX-ray2.80B/Q1-1203[»]
4C3HX-ray3.27B1-1203[»]
4C3IX-ray3.0B1-1203[»]
4C3JX-ray3.35B1-1203[»]
4YM7X-ray5.50AB/BB/CB/DB/EB/FB1-1203[»]
5G5Lelectron microscopy4.80B1-1203[»]
5LMXelectron microscopy4.90B1-1203[»]
5M3Felectron microscopy3.80B1-1203[»]
5M3Melectron microscopy4.00B1-1203[»]
5M5Welectron microscopy3.80B1-1203[»]
5M5Xelectron microscopy4.00B1-1203[»]
5M5Yelectron microscopy4.00B1-1203[»]
5M64electron microscopy4.60B1-1203[»]
5N5Yelectron microscopy7.70B1-1203[»]
5N5Zelectron microscopy7.70B1-1203[»]
5N60electron microscopy7.70B1-1203[»]
5N61electron microscopy3.40B1-1203[»]
5OA1electron microscopy4.40B1-1203[»]
5W5Yelectron microscopy3.80B1-1203[»]
5W64electron microscopy4.20B1-1203[»]
5W65electron microscopy4.30B1-1203[»]
5W66electron microscopy3.90B1-1203[»]
6H67electron microscopy3.60B1-1203[»]
6H68electron microscopy4.60B1-1203[»]
6HKOelectron microscopy3.42B1-1203[»]
6HLQelectron microscopy3.18B1-1203[»]
6HLRelectron microscopy3.18B1-1203[»]
6HLSelectron microscopy3.21B1-1203[»]
SMRiP22138
ModBaseiSearch...

Protein-protein interaction databases

BioGridi36188, 161 interactors
ComplexPortaliCPX-1664 DNA-directed RNA Polymerase I complex
DIPiDIP-135N
IntActiP22138, 60 interactors
MINTiP22138
STRINGi4932.YPR010C

PTM databases

iPTMnetiP22138

Proteomic databases

MaxQBiP22138
PaxDbiP22138
PRIDEiP22138

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR010C_mRNA; YPR010C_mRNA; YPR010C
GeneIDi856119
KEGGisce:YPR010C

Organism-specific databases

EuPathDBiFungiDB:YPR010C
SGDiS000006214 RPA135

Phylogenomic databases

GeneTreeiENSGT00950000183132
HOGENOMiHOG000222963
InParanoidiP22138
KOiK03002
OMAiFFGVVHY

Enzyme and pathway databases

BioCyciYEAST:G3O-34172-MONOMER
ReactomeiR-SCE-73762 RNA Polymerase I Transcription Initiation
R-SCE-73772 RNA Polymerase I Promoter Escape

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P22138

Family and domain databases

CDDicd00653 RNA_pol_B_RPB2, 1 hit
Gene3Di2.40.270.10, 1 hit
2.40.50.150, 1 hit
3.90.1110.10, 1 hit
InterProiView protein in InterPro
IPR015712 DNA-dir_RNA_pol_su2
IPR007120 DNA-dir_RNAP_su2_dom
IPR037033 DNA-dir_RNAP_su2_hyb_sf
IPR007121 RNA_pol_bsu_CS
IPR007644 RNA_pol_bsu_protrusion
IPR007642 RNA_pol_Rpb2_2
IPR037034 RNA_pol_Rpb2_2_sf
IPR007645 RNA_pol_Rpb2_3
IPR007641 RNA_pol_Rpb2_7
IPR014724 RNA_pol_RPB2_OB-fold
IPR009674 Rpa2_dom_4
PANTHERiPTHR20856 PTHR20856, 1 hit
PfamiView protein in Pfam
PF06883 RNA_pol_Rpa2_4, 1 hit
PF04563 RNA_pol_Rpb2_1, 1 hit
PF04561 RNA_pol_Rpb2_2, 1 hit
PF04565 RNA_pol_Rpb2_3, 1 hit
PF00562 RNA_pol_Rpb2_6, 1 hit
PF04560 RNA_pol_Rpb2_7, 1 hit
PROSITEiView protein in PROSITE
PS01166 RNA_POL_BETA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRPA2_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P22138
Secondary accession number(s): D6W421
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: July 31, 2019
This is version 183 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
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